Expression of Synthetic Human Lysozyme Gene in Escherichia coli
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概要
- 論文の詳細を見る
A 418 base pair DNA duplex consisting of a gene for human lysozyme with a synthetic ribosome binding site of E.coli was assembled by stepwise ligation of 56 chemically synthesized oligodeoxyribonucleotides. The synthesized gene was expressed under the control of the lambda pRpL promoter and the gene product accumulated as several percent of the total cellular proteins in E. coli. The expressed product existed as insoluble and biologically inactive aggregates in the cells, but the biological activity was regenerated by solubilization and renaturation of the aggregated protein. The results of the N-terminal amino acid sequence analysis of the product showed the human lysozyme synthesized in E. coli has an additional methionine residue at the N-terminal of the mature human lysozyme due to the translational initiation codon of E. coli.
- 社団法人 日本農芸化学会の論文
著者
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Harada Nobuhiro
National Chemical Laboratory For Industry
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JIGAMI Yoshifumi
National Chemical Laboratory for Industry
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TANAKA Hideaki
National Chemical Laboratory for Industry
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NAKASATO Satoshi
National Chemical Laboratory for Industry
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MURAKI Michiro
National Chemical Laboratory for Industry
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KISHIMOTO Fumitaka
Institute for Biological Science of Sumitomo Chemical Company
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AGUI Hideo
Institute for Biological Science of Sumitomo Chemical Company
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OGINO Shigeo
Institute for Biological Science of Sumitomo Chemical Company
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